Q3T1J2 (MBOA2_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Membrane-bound O-acyltransferase domain-containing protein 2
Short name=O-acyltransferase domain-containing protein 2
EC=2.3.-.-

Gene names

Name:	Mboat2
Synonyms:	Oact2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	519 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle By similarity.
Pathway	Lipid metabolism; phospholipid metabolism.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Sequence similarities	Belongs to the membrane-bound acyltransferase family.
Sequence caution	The sequence BC101889 differs from that shown. Reason: Frameshift at position 41.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	transferase activity, transferring acyl groups Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 519	519	Membrane-bound O-acyltransferase domain-containing protein 2		PRO_0000273022
Regions
	Transmembrane	22 – 42	21	Helical; Potential
	Transmembrane	61 – 81	21	Helical; Potential
	Transmembrane	88 – 108	21	Helical; Potential
	Transmembrane	184 – 204	21	Helical; Potential
	Transmembrane	236 – 256	21	Helical; Potential
	Transmembrane	288 – 305	18	Helical; Potential
	Transmembrane	365 – 385	21	Helical; Potential
	Transmembrane	415 – 435	21	Helical; Potential
	Transmembrane	443 – 463	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q3T1J2 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: D5CAFBD16F7642B3	FASTA	519	59,001
	10 20 30 40 50 60 MATTSTTGST LLQPLSNAVQ LPIDQVNFVV CQLFALLAAV WFRTYLHSSK TSSFIRHVVA 70 80 90 100 110 120 TLLGLYLAFF CFGWYALHFL VQSGISYCIM IIAGVESMHQ CCFVFALGYL SVCQITRVYI 130 140 150 160 170 180 FDYGQYSADF SGPMMIITQK ITSLAYEIHD GMFRKDEELT PSQRGLAVRR MPSLLEYVSY 190 200 210 220 230 240 TCNFMGILAG PLCSYKDYIA FIEGRASHMA QSGENGKEEQ HGKAEPSPNA AVTEKLLVCG 250 260 270 280 290 300 LSLLFHLTIS SMLPVEYNID EHFQATASWP TKATYLYVSL LAARPKYYFA WTLADAINNA 310 320 330 340 350 360 AGFGFRGYDK NGVARWDLIS NLRIQQIEMS TSFKMFLDNW NIQTALWLKR VCYERATFSP 370 380 390 400 410 420 TVQTFFLSAI WHGVYPGYYL TFLTGVLMTL AARAVRNNFR HYFVEPPQLK LFYDIITWAA 430 440 450 460 470 480 TQITISYTVV PFVLLSINPS FTFYRSWYYC LHICSILVLL LLPVKKSPRK KNTEENAQPS 490 500 510 WAKKFDEREN SLGQNSFSMM NNVCNQNQDT GSRHSALTQ

References

[1]

"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.

[2]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AABR03049793 Genomic DNA. No translation available. AABR03054282 Genomic DNA. No translation available. AABR03052483 Genomic DNA. No translation available. AABR03050975 Genomic DNA. No translation available. AABR03049616 Genomic DNA. No translation available. BC101889 mRNA. No translation available.
IPI	IPI00366862.
RefSeq	NP_001101486.2. NM_001108016.2.
UniGene	Rn.35322.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000009018.
Proteomic databases
PaxDb	Q3T1J2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	313997.
KEGG	rno:313997.
Organism-specific databases
CTD	129642.
RGD	1305798. Mboat2.
Phylogenomic databases
eggNOG	COG5202.
HOGENOM	HOG000015994.
HOVERGEN	HBG058823.
InParanoid	Q3T1J2.
KO	K13517.
OrthoDB	EOG4N5VWQ.
Enzyme and pathway databases
UniPathway	UPA00085.
Gene expression databases
ArrayExpress	Q3T1J2.
Genevestigator	Q3T1J2.
Family and domain databases
InterPro	IPR004299. MBOAT_fam. [Graphical view]
Pfam	PF03062. MBOAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	667109.

Entry information

Entry name

MBOA2_RAT

Accession

Primary (citable) accession number: Q3T1J2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 50 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program